ID C7NKP1_KYTSD Unreviewed; 371 AA.
AC C7NKP1;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Pyruvate/2-oxoglutarate dehydrogenase complex, dehydrogenase component alpha subunit {ECO:0000313|EMBL:ACV05527.1};
GN OrderedLocusNames=Ksed_04540 {ECO:0000313|EMBL:ACV05527.1};
OS Kytococcus sedentarius (strain ATCC 14392 / DSM 20547 / CCM 314 / 541)
OS (Micrococcus sedentarius).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Kytococcaceae;
OC Kytococcus.
OX NCBI_TaxID=478801 {ECO:0000313|EMBL:ACV05527.1, ECO:0000313|Proteomes:UP000006666};
RN [1] {ECO:0000313|EMBL:ACV05527.1, ECO:0000313|Proteomes:UP000006666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14392 / DSM 20547 / CCM 314 / 541
RC {ECO:0000313|Proteomes:UP000006666};
RX PubMed=21304632; DOI=10.4056/sigs.761;
RA Sims D., Brettin T., Detter J.C., Han C., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., Cheng J.F.,
RA Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., Ivanova N.,
RA Mavrommatis K., Chen A., Palaniappan K., D'haeseleer P., Chain P.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Schneider S.,
RA Goker M., Pukall R., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Kytococcus sedentarius type strain (541).";
RL Stand. Genomic Sci. 1:12-20(2009).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; CP001686; ACV05527.1; -; Genomic_DNA.
DR RefSeq; WP_012801945.1; NC_013169.1.
DR AlphaFoldDB; C7NKP1; -.
DR STRING; 478801.Ksed_04540; -.
DR KEGG; kse:Ksed_04540; -.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_029393_1_0_11; -.
DR Proteomes; UP000006666; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR017596; PdhA/BkdA.
DR InterPro; IPR029061; THDP-binding.
DR NCBIfam; TIGR03181; PDH_E1_alph_x; 1.
DR PANTHER; PTHR43380; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43380:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR Pfam; PF00676; E1_dh; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:ACV05527.1}.
FT DOMAIN 45..316
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 351..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 371 AA; 39780 MW; 7199F10E376CED60 CRC64;
MPSPQDLLPS EEPVQFIAPG GELTASDHPR GYTLPEPGRL LALYRGMVLG RRFDKQATAL
TKQGRLAVYP SSYGQDACQV ATVQALREDD WFFPTYRDSM ALVTRGIDPV QVLTLLKGDW
HAGYDVAATR TAPQCTPLAT QLIHAAGAGA GAARKGSDAA VLAFIGDGAT SEGDFHEGLN
FAAVFNAPVV FVVQNNTYAI SVPLSKQTKA PSLAYKGIGY GIPSEQVDGN DAAAVAAVMD
SALARARSGG GPTLVELHTY RLDAHTNADD ATRYRASDEV EGWLTKDPIV RLEQYLLATG
ALDEARIEEI RAEGEEQSAA LRDRMNADVE HQPLDLFDHV FTNPTAQLTE QRAQVAAEMA
ASAENDQEAA R
//
